ISSN:
1573-4919
Keywords:
ADP-ribosyltransferase
;
elongation factor 2
;
protein synthesis
;
bacterial toxins
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
Notes:
Abstract A cellular ADP-ribosyltransferase activity has been found in a variety of animals and tissues. The enzyme transfers ADP-ribose from NAD to elongation factor 2, inactivating the factor and thus inhibitingin vitro protein synthesis. Although, the mechanism of action of the cellular enzyme appears similar to diphtheria toxin andPseudomonas exotoxin A, it differs from the toxins in that only a fraction of the EF-2 pool is modified. The endogenously ADP-ribosylated EF-2 has been detected by a variety of methods including two-dimensional electrophoresis and immunoprecipitation with elongation factor 2 antibody. The nature of the cellular ADP-ribosyltransferase and its physiological significance are unknown.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00928454
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